1zbf

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(New page: 200px<br /><applet load="1zbf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zbf, resolution 1.50&Aring;" /> '''Crystal structure of...)
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[[Image:1zbf.gif|left|200px]]<br /><applet load="1zbf" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zbf.gif|left|200px]]<br /><applet load="1zbf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zbf, resolution 1.50&Aring;" />
caption="1zbf, resolution 1.50&Aring;" />
'''Crystal structure of B. halodurans RNase H catalytic domain mutant D132N'''<br />
'''Crystal structure of B. halodurans RNase H catalytic domain mutant D132N'''<br />
==Overview==
==Overview==
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RNase H belongs to a nucleotidyl-transferase superfamily, which includes, transposase, retroviral integrase, Holliday junction resolvase, and RISC, nuclease Argonaute. We report the crystal structures of RNase H complexed, with an RNA/DNA hybrid and a mechanism for substrate recognition and, two-metal-ion-dependent catalysis. RNase H specifically recognizes the A, form RNA strand and the B form DNA strand. Structure comparisons lead us, to predict the catalytic residues of Argonaute and conclude that, two-metal-ion catalysis is a general feature of the superfamily. In, nucleases, the two metal ions are asymmetrically coordinated and have, distinct roles in activating the nucleophile and stabilizing the, transition state. In transposases, they are symmetrically coordinated and, exchange roles to alternately activate a water and a 3'-OH for successive, strand cleavage and transfer by a ping-pong mechanism.
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RNase H belongs to a nucleotidyl-transferase superfamily, which includes transposase, retroviral integrase, Holliday junction resolvase, and RISC nuclease Argonaute. We report the crystal structures of RNase H complexed with an RNA/DNA hybrid and a mechanism for substrate recognition and two-metal-ion-dependent catalysis. RNase H specifically recognizes the A form RNA strand and the B form DNA strand. Structure comparisons lead us to predict the catalytic residues of Argonaute and conclude that two-metal-ion catalysis is a general feature of the superfamily. In nucleases, the two metal ions are asymmetrically coordinated and have distinct roles in activating the nucleophile and stabilizing the transition state. In transposases, they are symmetrically coordinated and exchange roles to alternately activate a water and a 3'-OH for successive strand cleavage and transfer by a ping-pong mechanism.
==About this Structure==
==About this Structure==
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1ZBF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halodurans Bacillus halodurans] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZBF OCA].
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1ZBF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halodurans Bacillus halodurans] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZBF OCA].
==Reference==
==Reference==
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[[Category: Ribonuclease H]]
[[Category: Ribonuclease H]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Crouch, R.J.]]
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[[Category: Crouch, R J.]]
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[[Category: Gaidamakov, S.A.]]
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[[Category: Gaidamakov, S A.]]
[[Category: Nowotny, M.]]
[[Category: Nowotny, M.]]
[[Category: Yang, W.]]
[[Category: Yang, W.]]
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[[Category: rnase h]]
[[Category: rnase h]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:21:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:56 2008''

Revision as of 14:13, 21 February 2008


1zbf, resolution 1.50Å

Drag the structure with the mouse to rotate

Crystal structure of B. halodurans RNase H catalytic domain mutant D132N

Overview

RNase H belongs to a nucleotidyl-transferase superfamily, which includes transposase, retroviral integrase, Holliday junction resolvase, and RISC nuclease Argonaute. We report the crystal structures of RNase H complexed with an RNA/DNA hybrid and a mechanism for substrate recognition and two-metal-ion-dependent catalysis. RNase H specifically recognizes the A form RNA strand and the B form DNA strand. Structure comparisons lead us to predict the catalytic residues of Argonaute and conclude that two-metal-ion catalysis is a general feature of the superfamily. In nucleases, the two metal ions are asymmetrically coordinated and have distinct roles in activating the nucleophile and stabilizing the transition state. In transposases, they are symmetrically coordinated and exchange roles to alternately activate a water and a 3'-OH for successive strand cleavage and transfer by a ping-pong mechanism.

About this Structure

1ZBF is a Single protein structure of sequence from Bacillus halodurans with as ligand. Active as Ribonuclease H, with EC number 3.1.26.4 Full crystallographic information is available from OCA.

Reference

Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis., Nowotny M, Gaidamakov SA, Crouch RJ, Yang W, Cell. 2005 Jul 1;121(7):1005-16. PMID:15989951

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